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. 1975 Sep;72(9):3428–3432. doi: 10.1073/pnas.72.9.3428

Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli.

J Rouvière-Yaniv, F Gros
PMCID: PMC433007  PMID: 1103148

Abstract

A low-molecular-weight (7000), heat-stable protein--HU--that stimulates transcription of bacteriophage lambda DNA by E. coli RNA polymerase was purified from E. coli extracts using affinity chromatography on DNA-cellulose. HU binds to native DNA, resulting in an apparent thickening of the DNA chains as revealed by electron microscopy. Contrary to DNA unwinding proteins, it causes no destabilization of the double helix. HU differs from previously described transcription factors (H1, D, etc.) and from the low-molecular-weight omega subunit of the RNA polymerase. By its amino-acid composition and characteristics, HU displays an interesting resemblance to some eukaryotic histones, such as H2B and H1.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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